ID F6FUQ8_ISOV2 Unreviewed; 289 AA.
AC F6FUQ8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Citryl-CoA lyase {ECO:0000313|EMBL:AEG43319.1};
DE EC=4.1.3.34 {ECO:0000313|EMBL:AEG43319.1};
GN OrderedLocusNames=Isova_0523 {ECO:0000313|EMBL:AEG43319.1};
OS Isoptericola variabilis (strain 225).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=743718 {ECO:0000313|Proteomes:UP000009236};
RN [1] {ECO:0000313|EMBL:AEG43319.1, ECO:0000313|Proteomes:UP000009236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=225 {ECO:0000313|Proteomes:UP000009236};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Zeytun A., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Siebers A., Allgaier M., Thelen M.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Isoptericola variabilis 225.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002810; AEG43319.1; -; Genomic_DNA.
DR RefSeq; WP_013837714.1; NC_015588.1.
DR AlphaFoldDB; F6FUQ8; -.
DR STRING; 743718.Isova_0523; -.
DR KEGG; iva:Isova_0523; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_2_1_11; -.
DR Proteomes; UP000009236; Chromosome.
DR GO; GO:0008816; F:citryl-CoA lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR32308:SF10; CITRATE LYASE SUBUNIT BETA; 1.
DR PANTHER; PTHR32308; LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-RELATED; 1.
DR Pfam; PF03328; HpcH_HpaI; 2.
DR PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:AEG43319.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR015582-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009236}.
FT DOMAIN 12..96
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT DOMAIN 111..217
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 289 AA; 29771 MW; F7F4FE64AC8B8B8C CRC64;
MTPPPFTLGP ALLFCPADRP DRYVKALDRA DAVILDLEDA VARDRKEAAR QALVDHPVDP
DRTIVRVNAV GTPDHADDLA ALARTAYRTI MLPKADGTFV GPLLGPDGGP YAVVALCETA
AGVLAAPALA ARPDIVALAW GAEDLVASLG GTSSRRADGT YRDVARYARS AVLVAAAATG
KAAIDAVHLD IGDLDGLRAE AADAVAVGFA ATMCIHPSHA DVIRAAYAPS DEKVAEAREV
VGAARRAASA GAGVLTVGGR MVDAPLVRHA EAVLRRAGWQ DRSGDDAAP
//
